Xanthine dehydrogenase - Drosophila pseudoobscura pseudoobscura (Fruit fly)

Names and origin

Protein names

Recommended name:
    Xanthine dehydrogenase
      Short name=XD
    EC=1.17.1.4
Alternative name(s):
    Protein rosy locus

Gene names

Name:	ry
Synonyms:	XDH
ORF Names:	GA20500

Organism

Drosophila pseudoobscura pseudoobscura (Fruit fly) [Complete proteome]

Taxonomic identifier

46245 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length	1343 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Catalytic activity	Xanthine + NAD⁺ + H₂O = urate + NADH. Hypoxanthine + NAD⁺ + H₂O = xanthine + NADH.
Cofactor	Binds 2 2Fe-2S clusters. FAD. Molybdopterin.
Subunit structure	Homodimer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.

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Ontologies

Keywords
Cellular component	Peroxisome
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW xanthine dehydrogenase activity Inferred from electronic annotation. Source: EC xanthine oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1343

1343

Xanthine dehydrogenase

PRO_0000166080

Regions

Domain

8 – 95

88

2Fe-2S ferredoxin-type

Domain

235 – 424

190

FAD-binding PCMH-type

Sites

Metal binding

41

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

47

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

52

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

55

1

Iron-sulfur (2Fe-2S) By similarity

Experimental info

Sequence conflict

58

1

V → M in AAA29022. Ref.1

Sequence conflict

200

1

T → A in AAA29022. Ref.1

Sequence conflict

428

1

V → I in AAA29022. Ref.1

Sequence conflict

428

1

V → I in AAX13180. Ref.3

Sequence conflict

461

1

G → E in AAA29022. Ref.1

Sequence conflict

461

1

G → E in AAX13180. Ref.3

Sequence conflict

475

1

L → V in AAA29022. Ref.1

Sequence conflict

734

1

E → D in AAX13180. Ref.3

Sequence conflict

747

1

S → N in AAA29022. Ref.1

Sequence conflict

762

1

A → G in AAA29022. Ref.1

Sequence conflict

986

1

A → V in AAX13180. Ref.3

Sequence conflict

1245

1

Missing in AAA29022. Ref.1

Sequence conflict

1320

1

C → F in AAA29022. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P22811-1 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: A58C142336E14BC9
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FASTA

1,343

147,349

        10         20         30         40         50         60 
MSGQQKTSEL VFFVNGKKVT DTNPDPECTL LTYLRDKLRL CGTKLGCAEG GCGACTVVIS 

        70         80         90        100        110        120 
RMDRGQNKIR HLAVNACLTP VCAMHGCAVT TVEGIGSTRT RLHPVQERLA KAHGSQCGFC 

       130        140        150        160        170        180 
TPGIVMSMYA LLRSAEQPSM RDLEVAFQGN LCRCTGYRPI LEGYKTFTKE FACGMGDKCC 

       190        200        210        220        230        240 
KVNGKGCGGG DDTQSVTDDT LFERSQFQPL DPSQEPIFPP ELQLTPTYDS ESLIFSSERV 

       250        260        270        280        290        300 
TWYRPTTLQE LLQLKSDHPS AKLVVGNTEV GVEVKFKHFL YPHLINPTQV PELLEVRESE 

       310        320        330        340        350        360 
ESIYFGAAVS LMEIDALLRQ RIEELPEAQT RLFQCAVDML HYFAGKQIRN VACLGGNIMT 

       370        380        390        400        410        420 
GSPISDMNPV LTAAGARLEV ASLVGGKTSH RTVHMGTGFF TGYRRNVIEP HEVLLGIHFQ 

       430        440        450        460        470        480 
KTTPDQHVVA FKQARRRDDD IAIVNAAVNV RFEPRTNVVA GISMAFGGMA PTTVLAPRTS 

       490        500        510        520        530        540 
QLMVKQPLDH HLVERVAESL CGELPLAASA PGGMIAYRRA LVVSLIFKAY LSISRKLSEA 

       550        560        570        580        590        600 
GIISTDAIPA EERSGAELFH TPVLRSAQLF ERVCSEQPVC DPIGRPEVHA AALKQATGEA 

       610        620        630        640        650        660 
IYTDDIPRMD GELYLGLVLS TKPRAKITKL DASEALALEG VHAFFSHKDL TEHENEVGPV 

       670        680        690        700        710        720 
FHDEHVFAAA EVHCYGQIVG AVAADNKALA QRAARLVRVE YEELAPVIVT IEQAIEHGSY 

       730        740        750        760        770        780 
FPDYPRYVNK GNVEEAFAAA EHTYEGSCRM GGQEHFYLET HAAVAVPRDS DELELFCSTQ 

       790        800        810        820        830        840 
HPSEVQKLVA HVTTLPAHRV VCRAKRLGGG FGGKESRGIS VALPVALAAY RLRRPVRCML 

       850        860        870        880        890        900 
DRDEDMLITG TRHPFLFKYK VAFASDGLIT ACDIECYNNA GWSMDLSFSV LERAMYHFEN 

       910        920        930        940        950        960 
CYRIPNVRVG GWVCKTNLPS NTAFRGFGGP QGMFAGEHII RDVARIVGRD VLDVMRLNFY 

       970        980        990       1000       1010       1020 
KTGDITHYNQ KLEHFPIERC LDDCLAQSRY HEKRTEIAKF NRENRWRKRG MAVIPTKYGI 

      1030       1040       1050       1060       1070       1080 
AFGVMHLNQA GALINVYGDG SVLLSHGGVE IGQGLNTKMI QCAARALGIP IELIHISETA 

      1090       1100       1110       1120       1130       1140 
TDKVPNTSPT AASVGSDLNG MAVLDACEKL NKRLAPIKEA LPQGTWQEWI NKAYFDRVSL 

      1150       1160       1170       1180       1190       1200 
SATGFYAMPG IGYHPETNPN ARTYSYYTNG VGISVVEIDC LTGDHQVLST DIVMDIGSSI 

      1210       1220       1230       1240       1250       1260 
NPAIDIGQIE GAFMQGYGLF TLEELMYSPQ GMLYSRGPGM YKLPGFADIP GEFNVSLLTG 

      1270       1280       1290       1300       1310       1320 
APNPRAVYSS KAVGEPPLFI GSSAFFAIKE AIAAARQEQG LTGDFPLEAP STSARIRMAC 

      1330       1340 
QDKFTNLLEI PEEGSFTPWN IVP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Xdh region in Drosophila pseudoobscura and an analysis of the evolution of synonymous codons." Riley M.A. Mol. Biol. Evol. 6:33-52(1989) [PubMed: 2493563] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution." Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L. Gibbs R.A. Genome Res. 15:1-18(2005) [PubMed: 15632085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MV2-25.
[3]	"Patterns of selection on synonymous and nonsynonymous variants in Drosophila miranda." Bartolome C., Maside X., Yi S., Grant A.L., Charlesworth B. Genetics 169:1495-1507(2005) [PubMed: 15545653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-1062.

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Cross-references

Sequence databases
	M33977 Genomic DNA. Translation: AAA29022.1. CM000070 Genomic DNA. Translation: EAL27642.2. AY754605 Genomic DNA. Translation: AAX13180.1.
PIR	A31946.
RefSeq	XP_001358503.2.
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Genome annotation databases
GeneID	4801405.
KEGG	dpo:Dpse_GA20500.
Organism-specific databases
FlyBase	FBgn0012736. Dpse\ry.
Enzyme and pathway databases
BRENDA	1.17.1.4. 190795.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR016208. Ald_Oxase/xanthine_DH. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR012675. b-grasp_ferredoxin-like. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR001041. Ferredoxin. IPR002346. Mopterin_DH_FAD-bd. IPR000572. OxRdtase_Mopterin-bd. IPR014307. Xanthine_DH_ssu. [Graphical view]
Gene3D	G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF01315. Ald_Xan_dh_C. 1 hit. PF02738. Ald_Xan_dh_C2. 1 hit. PF03450. CO_deh_flav_C. 1 hit. PF00941. FAD_binding_5. 1 hit. PF00111. Fer2. 1 hit. PF01799. Fer2_2. 1 hit. [Graphical view]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02963. xanthine_xdhA. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

XDH_DROPS

Accession

Primary (citable) accession number: P22811
Secondary accession number(s): Q299Q9, Q56RA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	July 11, 2006
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents